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Swabia® Nutrition

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Nutriceuticals

Discovery of Salt Taste Enhancing Arginyl Dipeptides in Protein Digests and Fermented Fish Sauces by Means of a Sensomics Approach

A Schindler et al. J Agric Food Chem 59 (23), 12578-12588. 2011 Nov 14.


Salt Taste Enhancing L-Arginyl Dipeptides From Casein and Lysozyme Released by Peptidases of Basidiomycota

L Harth et al. J Agric Food Chem. 2016 Aug 24.


A Series of Kokumi Peptides Impart the Long-Lasting Mouthfulness of Matured Gouda Cheese

S Toelstede et al. J Agric Food Chem 57 (4), 1440-1448. 2009 Feb 25.


Abstract

Among the gamma-L-glutamyl peptides, the candidates gamma-Glu-Glu, gamma-Glu-Gly, gamma-Glu-Gln, gamma-Glu-Met, gamma-Glu-Leu, and gamma-Glu-His, present in GC44 in concentrations between 4.11 and 17.66 micromol/kg, were identified for the first time as the key kokumi molecules enhancing mouthfulness and complex taste continuity of the matured cheese.


A total of 10 kokumi peptides were identified from yeast extract. They were γ-Glu-Cys-Gly, γ-Glu-Leu, γ-Glu-Val, γ-Glu-Tyr, Leu-Lys, Leu-Gln, Leu-Ala, Leu-Glu, Leu-Thr and Ala-Leu. Apart from the well-known kokumi-active glutathione and γ-glutamyl dipeptides, five leucyl dipeptides were first proposed having kokumi activity. Among them, Ala-Leu was found to have the highest kokumi threshold concentration .

Alteration of the Substrate Specificity of L-Amino Acid Ligase and Selective Synthesis of Met-Gly as a Salt Taste Enhancer

H Kino et al. Biosci Biotechnol Biochem 79 (11), 1827-1832. 2015 Jun 19.

Effective Production of Pro-Gly by Mutagenesis of L-Amino Acid Ligase

H Kino et al. J Biosci Bioeng 122 (2), 155-159. 2016 Mar 24.

Abstract

l-Amino acid ligase (Lal) catalyzes dipeptide synthesis from unprotected l-amino acids by hydrolysis ATP to ADP. Each Lal displays unique substrate specificity, and many different dipeptides can be synthesized by selecting suitable Lal. We have already successfully synthesized Met-Gly selectively by replacing the Pro85 residues of Lal from Bacillus licheniformis (BL00235).

Verwendung von tryptophanhaltigen Peptiden mit blutdrucksenkender und vasoprotektiver Wirkung für die Herstellung  biofunktioneller Lebensmittel.


Molkenproteinhydrolysat mit ACE-hemmender und antihypertensiver Wirkung enthält eine physiologisch wirksame Menge mindestens eines der bioaktiven Dipeptide Ile-Trp und Trp-Leu .


Die Herstellung der damit angereicherten Molkenproteinhydrolysate (whey protein)  ist zugänglich  durch extensive Hydrolyse von Molkenproteinisolaten bzw. reinem α-Lactalbumin.


Ebenso besteht außerdem die Möglichkeit, die Herstellung  von Nahrungsergänzungsmitteln und Nahrungsprodukten, durch definierte Zugabe synthetisch hergestellter Dipeptide  nach eigener Rezeptur zu realisieren.


References

SATO,M.,et.al.: Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Wakame (Undaria pinnatifida) and Their Anthiypertensive Effect in Spontaneously Hypertensive Rats.In: American Chemical Society,2002,50,S.6245-6252

KUBA,Megumi,et.al.: Angiotensin I-Converting Enzyme Inhibitory Peptides Isolated from Tofuyo Fermented Soybean Food. In: Biosci. Biotechnol.Biochem.67,6,2003,S.1278-1283

MULLALLY,Margaret M.,et.al.: Synthetic Peptides Corresponding to alpha-lactalbumin and ß-Lactoglobulin Sequences with Angiotensin-I-Converting Enzyme Inhibitory Activity. In: Biol.Chem.Hoppe-Seyler ,Vol.377,S.259-260,April 1996
BIOSIS Abstracts Prev.20000134824

Synthetic Dipeptides -  A New Dimension in Clinical Nutrition / Novel Food

Prof.Peter Fürst, MD, PhD.
Institute of Biological Chemistry and Nutrition, University of Hohenheim, Stuttgart /Germany.


Dipeptide utilization - human studies
Human studies in healthy volunteers demonstrated that the synthetic glutamine dipeptides L-glutamine (Ala-Gln, present in Dipeptiven®) and glycyl-L-glutamine (Gly-Gin, Present in Glamin®) as well as the synthetic tyrosine dipeptide glycyl-L-tyrosine (Gly-Tyr, present in Glamin®) are rapidly hydrolyzed after bolus injection (elimination half lives 3., 7.8, and 3.8 min, respectively). Continuous infusion of a commercial amino acid solution supplemented with Ala-Gln or Gly-Gln was not accompanied by any side effects, and no complaints were reported. Infusion of peptide-supplemented solutions resulted in a prompt increase in alanine, glutamine, tyrosine and glycine concentrations. During the entire infusion period, only trace amounts of the dipeptides could be measured in plasma. Urinary losses of dipeptids were only approximately 1% of the given dose. These results indicate a near-quantitative hydrolysis of the infused peptide, with subsequent utilization of the constituent free amino acids.

Phenylalanine and tyrosine metabolism in renal failure: Dipeptides as tyrosine source / Novel Food

Druml, Wilfried; Roth, Erich; Lenz, Kurt; Lochs, Herbert; Kopsa, Herbert, Kidney International Supplement;Nov1989, Issue 27, p282


Oral tyrosine supplementation was shown to replete plasma and intracellular pools and improve nitrogen balance in chronic renal failure patients on a low protein diet. However, because of poor solubility in aqueous solutions, tyrosine cannot be included in the free form in amino acid solutions for parenteral nutrition. To circumvent stability or solubility problems, tyrosine containing dipeptides and/or N-acetyl-tyrosine may serve as tyrosine sources for parenteral supply. Renal failure does not affect alanyl-tyrosine hydrolysis, and there is an immediate increase of plasma tyrosine concentration after peptide infusion. Elimination and hydrolysis of glycine-tyrosine is retarded in renal failure, but the clearance exceeds clinically relevant infusion rates. After infusion of N-acetyl-tyrosine, no increase in plasma tyrosine is seen, and the half-life N-acetyl-tyrosine is grossly prolonged in uremia. Thus, alanyl-tyrosine and glycyl-tyrosine. but not N-acetyl-tyrosine, are excellent tyrosine sources for parenteral nutrition. For the first time, the use of dipeptides permits adequate tyrosine supplementation for uremic patients on parenteral nutritional support.

Angiotensin converting enzyme inhibitory peptides from a lactotripeptide-enriched milk beverage are absorbed intact into the circulation. / Novel Food

Foltz M1, Meynen EE, Bianco V, van Platerink C, Koning TM, Kloek J. ,J Nutr. 2007 Apr;137(4):953-8.


Food products containing angiotensin converting enzyme (ACE) inhibitory peptides reportedly play a role in treatment of mild hypertension. The aim of this placebo-controlled crossover study was to assess the bioavailability of Ile-Pro-Pro and 7 other ACE-inhibiting peptides present in a lactotripeptide (LTP)-enriched yogurt beverage and whether meal intake affects Ile-Pro-Pro bioavailability.  Meal intake affected Ile-Pro-Pro concentrations. When the beverage was consumed after a meal, the AUC of Ile-Pro-Pro was 1.3-fold (P < 0.05) of the AUC derived from premeal intake. This was due to an increase in the plasma elimination half-life (P < 0.05); C(max) and T(max) were not affected by meal intake. In summary, this is the first demonstration, to our knowledge, that the tripeptide Ile-Pro-Pro selectively escapes from intestinal degradation and reaches the circulation undegraded.

Lactotripeptides

are two naturally occurring milk peptides: Isoleucine-Proline-Proline (IPP) and Valine-Proline-Proline (VPP). These lactotripeptides are derived from casein, which is a milk protein also found in dairy products. Although most normal dairy products contain lactotripeptides, they are inactive within the original milk proteins. Dairy peptides can be effectively released through enzymatic predigestion – a process by which milk protein is enzymatically broken down into smaller pieces.

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